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Volumn 394, Issue 1, 2006, Pages 11-17

Evolutionary conserved structural motifs in bacterial GST (glutathione S-transferase) are involved in protein folding and stability

Author keywords

Bacterial glutathione S transferase (GST); Hydrophobic staple motif; N capping box; Proteus mirabilis GST B1 1 (PmGST B1 1); Site directed mutagenesis

Indexed keywords

CATALYSIS; ENZYMES; HYDROGEN BONDS; HYDROPHOBICITY; MUTAGENESIS; PROTEINS;

EID: 32944467164     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051367     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes, J. D. and Pulford, D. J. (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30, 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 2
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Hayes, J. D. and McLellan, L. I. (1999) Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Rad. Res. 31, 273-300
    • (1999) Free Rad. Res. , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 3
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong, R. N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10, 2-18
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 4
    • 0024269217 scopus 로고
    • Glutathione transferases: Structure and catalytic activity
    • Mannervik, B. and Danielson, U. H. (1988) Glutathione transferases: structure and catalytic activity. Crit. Rev. Biochem. Mol. Biol. 23, 283-337
    • (1988) Crit. Rev. Biochem. Mol. Biol. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 6
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan, D., Meade, G., Foley, V. M. and Dowd, C. A. (2001) Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360, 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 7
    • 0031045777 scopus 로고    scopus 로고
    • Identification of an N-capping box that affects the α6-helix propensity in glutathione S-transferase superfamily proteins: A role for an invariant aspartic residue
    • Aceto, A., Dragani, B., Melino, S., Allocati, N., Masulli, M., Di Ilio, C. and Petruzzelli, R. (1997) Identification of an N-capping box that affects the α6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue. Biochem. J. 322, 229-234
    • (1997) Biochem. J. , vol.322 , pp. 229-234
    • Aceto, A.1    Dragani, B.2    Melino, S.3    Allocati, N.4    Masulli, M.5    Di Ilio, C.6    Petruzzelli, R.7
  • 8
    • 0030824202 scopus 로고    scopus 로고
    • The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability
    • Dragani, B., Stenberg, G., Melino, S., Petruzzelli, R., Mannervik, B. and Aceto, A. (1997) The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability. J. Biol. Chem. 272, 25518-25523
    • (1997) J. Biol. Chem. , vol.272 , pp. 25518-25523
    • Dragani, B.1    Stenberg, G.2    Melino, S.3    Petruzzelli, R.4    Mannervik, B.5    Aceto, A.6
  • 9
    • 0034616347 scopus 로고    scopus 로고
    • A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase P1-1
    • Stenberg, G., Dragani, B., Cocco, R., Mannervik, B. and Aceto, A. (2000) A conserved 'hydrophobic staple motif' plays a crucial role in the refolding of human glutathione transferase P1-1. J. Biol. Chem. 275, 10421-10428
    • (2000) J. Biol. Chem. , vol.275 , pp. 10421-10428
    • Stenberg, G.1    Dragani, B.2    Cocco, R.3    Mannervik, B.4    Aceto, A.5
  • 10
    • 0035943609 scopus 로고    scopus 로고
    • The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif
    • Cocco, R., Stenberg, G., Dragani, B., Rossi Principe, D., Paludi, D., Mannervik, B. and Aceto, A. (2001) The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif. J. Biol. Chem. 276, 32177-32183
    • (2001) J. Biol. Chem. , vol.276 , pp. 32177-32183
    • Cocco, R.1    Stenberg, G.2    Dragani, B.3    Rossi Principe, D.4    Paludi, D.5    Mannervik, B.6    Aceto, A.7
  • 11
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: The capping box
    • Harper, E. T. and Rose, G. D. (1993) Helix stop signals in proteins and peptides: the capping box. Biochemistry 32, 7605-7609
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.T.1    Rose, G.D.2
  • 13
    • 0029009067 scopus 로고
    • The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding
    • Munoz, V., Blanco, F. J. and Serrano, L. (1995) The hydrophobic-staple motif and a role for loop-residues in alpha-helix stability and protein folding. Nat. Struct. Biol. 2, 380-385
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 380-385
    • Munoz, V.1    Blanco, F.J.2    Serrano, L.3
  • 14
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson, J. S. and Richardson, D. C. (1988) Amino acid preferences for specific locations at the ends of a helices. Science (Washington, D.C.) 240, 1648-1652
    • (1988) Science (Washington, D.C.) , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 16
    • 0027535337 scopus 로고
    • The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes
    • Mignogna, G., Allocati, N., Aceto, A., Piccolomini, R., Di Ilio, C., Barra, D. and Martini, F. (1993) The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes. Eur. J. Biochem. 211, 421-425
    • (1993) Eur. J. Biochem. , vol.211 , pp. 421-425
    • Mignogna, G.1    Allocati, N.2    Aceto, A.3    Piccolomini, R.4    Di Ilio, C.5    Barra, D.6    Martini, F.7
  • 19
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • Rossjohn, J., Polekhina, G., Feil, S. C., Allocati, N., Masulli, M., Di Ilio, C. and Parker, M. W. (1998) A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6, 721-734
    • (1998) Structure , vol.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    Di Ilio, C.6    Parker, M.W.7
  • 20
    • 0033021942 scopus 로고    scopus 로고
    • Functional of the evolutionary conserved proline 53 residue in Proteus mirabilis glutathione transferase B1-1
    • Allocati, N., Casalone, E., Masulli, M., Ceccarelli, I., Carletti, E., Parker, M. W. and Di Ilio, C. (1999) Functional of the evolutionary conserved proline 53 residue in Proteus mirabilis glutathione transferase B1-1. FEBS Lett. 445, 347-350
    • (1999) FEBS Lett. , vol.445 , pp. 347-350
    • Allocati, N.1    Casalone, E.2    Masulli, M.3    Ceccarelli, I.4    Carletti, E.5    Parker, M.W.6    Di Ilio, C.7
  • 21
    • 0034667663 scopus 로고    scopus 로고
    • Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases
    • Allocati, N., Casalone, E., Masulli, M., Polekhina, G., Rossjohn, J., Parker, M. W. and Di Ilio, C. (2000) Evaluation of the role of two conserved active-site residues in beta class glutathione S-transferases. Biochem J. 351, 341-346
    • (2000) Biochem J. , vol.351 , pp. 341-346
    • Allocati, N.1    Casalone, E.2    Masulli, M.3    Polekhina, G.4    Rossjohn, J.5    Parker, M.W.6    Di Ilio, C.7
  • 22
    • 0036534751 scopus 로고    scopus 로고
    • Glutamic acid 65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1
    • Allocati, N., Masulli, M., Casalone, E., Santucci, S., Favaloro, B., Parker, M. W. and Di Ilio, C. (2002) Glutamic acid 65 is an essential residue for catalysis in Proteus mirabilis glutathione S-transferase B1-1. Biochem J. 363, 189-193
    • (2002) Biochem J. , vol.363 , pp. 189-193
    • Allocati, N.1    Masulli, M.2    Casalone, E.3    Santucci, S.4    Favaloro, B.5    Parker, M.W.6    Di Ilio, C.7
  • 23
    • 12744260133 scopus 로고    scopus 로고
    • Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1
    • Allocati, N., Masulli, M., Pietracupa, M., Favaloro, B., Federici, L. and Di Ilio, C. (2005) Contribution of the two conserved tryptophan residues to the catalytic and structural properties of Proteus mirabilis glutathione S-transferase B1-1. Biochem J. 385, 37-43
    • (2005) Biochem J. , vol.385 , pp. 37-43
    • Allocati, N.1    Masulli, M.2    Pietracupa, M.3    Favaloro, B.4    Federici, L.5    Di Ilio, C.6
  • 26
    • 0038005094 scopus 로고    scopus 로고
    • Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses
    • Allocati, N., Favaloro, B., Masulli, M., Alexeyev, M. F. and Di Ilio, C. (2003) Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses. Biochem. J. 373, 305-311
    • (2003) Biochem. J. , vol.373 , pp. 305-311
    • Allocati, N.1    Favaloro, B.2    Masulli, M.3    Alexeyev, M.F.4    Di Ilio, C.5
  • 30
    • 0017669854 scopus 로고
    • Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography
    • Simons, P. C. and Vander Jagt, D. L. (1977) Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal Biochem. 82, 334-341
    • (1977) Anal Biochem. , vol.82 , pp. 334-341
    • Simons, P.C.1    Vander Jagt, D.L.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0019741605 scopus 로고
    • Assay for differentiation of glutathione S-transferases
    • Habig, W. H. and Jakoby, W. B. (1981) Assay for differentiation of glutathione S-transferases. Methods Enzymol. 77, 398-405
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 37
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a Tau class glutathione S-transferase from wheat active in herbicide detoxification
    • Thorn, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J. and Lapthorn, A. J. (2002) Structure of a Tau class glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry 41, 7008-7020
    • (2002) Biochemistry , vol.41 , pp. 7008-7020
    • Thorn, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 39
    • 0037163126 scopus 로고    scopus 로고
    • Functional divergence in the glutathione transferase superfamily in plants
    • Dixon, D. P., Davis, B. G. and Edwards, R. (2002) Functional divergence in the glutathione transferase superfamily in plants. J. Biol. Chem. 277, 30859-30869
    • (2002) J. Biol. Chem. , vol.277 , pp. 30859-30869
    • Dixon, D.P.1    Davis, B.G.2    Edwards, R.3
  • 40
    • 13444270611 scopus 로고    scopus 로고
    • Intra-subunit residue interactions from the protein surface to the active site of glutathione S-transferase AdGSTD3-3 impact on structure and enzyme properties
    • Wongtrakul, J., Sramala, I., Prapanthadara, L. and Ketterman, A. J. (2005) Intra-subunit residue interactions from the protein surface to the active site of glutathione S-transferase AdGSTD3-3 impact on structure and enzyme properties. Insect Biochem. Mol. Biol. 35, 197-205
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 197-205
    • Wongtrakul, J.1    Sramala, I.2    Prapanthadara, L.3    Ketterman, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.